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Relevant bibliographies by topics / Dynein arms

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Academic literature on the topic 'Dynein arms'

Author: Grafiati

Published: 18 May 2024

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Journal articles on the topic "Dynein arms"

1

DiBella, Linda M., Miho Sakato, Ramila S. Patel-King, Gregory J. Pazour, and Stephen M. King. "The LC7 Light Chains of Chlamydomonas Flagellar Dyneins Interact with Components Required for Both Motor Assembly and Regulation." Molecular Biology of the Cell 15, no. 10 (October 2004): 4633–46. http://dx.doi.org/10.1091/mbc.e04-06-0461.

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Members of the LC7/Roadblock family of light chains (LCs) have been found in both cytoplasmic and axonemal dyneins. LC7a was originally identified within Chlamydomonas outer arm dynein and associates with this motor's cargo-binding region. We describe here a novel member of this protein family, termed LC7b that is also present in the Chlamydomonas flagellum. Levels of LC7b are reduced ∼20% in axonemes isolated from strains lacking inner arm I1 and are ∼80% lower in the absence of the outer arms. When both dyneins are missing, LC7b levels are diminished to <10%. In oda9 axonemal extracts that completely lack outer arms, LC7b copurifies with inner arm I1, whereas in ida1 extracts that are devoid of I1 inner arms it associates with outer arm dynein. We also have observed that some LC7a is present in both isolated axonemes and purified 18S dynein from oda1, suggesting that it is also a component of both the outer arm and inner arm I1. Intriguingly, in axonemal extracts from the LC7a null mutant, oda15, which assembles ∼30% of its outer arms, LC7b fails to copurify with either dynein, suggesting that it interacts with LC7a. Furthermore, both the outer arm γ heavy chain and DC2 from the outer arm docking complex completely dissociate after salt extraction from oda15 axonemes. EDC cross-linking of purified dynein revealed that LC7b interacts with LC3, an outer dynein arm thioredoxin; DC2, an outer arm docking complex component; and also with the phosphoprotein IC138 from inner arm I1. These data suggest that LC7a stabilizes both the outer arms and inner arm I1 and that both LC7a and LC7b are involved in multiple intradynein interactions within both dyneins.

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Wang, Limei, Xuecheng Li, Guang Liu, and Junmin Pan. "FBB18 participates in preassembly of almost all axonemal dyneins ind of R2TP complex." PLOS Genetics 18, no. 8 (August 26, 2022): e1010374. http://dx.doi.org/10.1371/journal.pgen.1010374.

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Assembly of dynein arms requires cytoplasmic processes which are mediated by dynein preassembly factors (DNAAFs). CFAP298, which is conserved in organisms with motile cilia, is required for assembly of dynein arms but with obscure mechanisms. Here, we show that FBB18, a Chlamydomonas homologue of CFAP298, localizes to the cytoplasm and functions in folding/stabilization of almost all axonemal dyneins at the early steps of dynein preassembly. Mutation of FBB18 causes no or short cilia accompanied with partial loss of both outer and inner dynein arms. Comparative proteomics using 15N labeling suggests partial degradation of almost all axonemal dynein heavy chains (DHCs). A mutant mimicking a patient variant induces particular loss of DHCα. FBB18 associates with 9 DNAAFs and 14 out of 15 dynein HCs but not with IC1/IC2. FBB18 interacts with RuvBL1/2, components of the HSP90 co-chaperone R2TP complex but not the holo-R2TP complex. Further analysis suggests simultaneous formation of multiple DNAAF complexes involves dynein folding/stability and thus provides new insights into axonemal dynein preassembly.

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Yamamoto, Ryosuke, Kangkang Song, Haru-aki Yanagisawa, Laura Fox, Toshiki Yagi, Maureen Wirschell, Masafumi Hirono, Ritsu Kamiya, Daniela Nicastro, and Winfield S. Sale. "The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility." Journal of Cell Biology 201, no. 2 (April 8, 2013): 263–78. http://dx.doi.org/10.1083/jcb.201211048.

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Axonemal dyneins must be precisely regulated and coordinated to produce ordered ciliary/flagellar motility, but how this is achieved is not understood. We analyzed two Chlamydomonas reinhardtii mutants, mia1 and mia2, which display slow swimming and low flagellar beat frequency. We found that the MIA1 and MIA2 genes encode conserved coiled-coil proteins, FAP100 and FAP73, respectively, which form the modifier of inner arms (MIA) complex in flagella. Cryo–electron tomography of mia mutant axonemes revealed that the MIA complex was located immediately distal to the intermediate/light chain complex of I1 dynein and structurally appeared to connect with the nexin–dynein regulatory complex. In axonemes from mutants that lack both the outer dynein arms and the MIA complex, I1 dynein failed to assemble, suggesting physical interactions between these three axonemal complexes and a role for the MIA complex in the stable assembly of I1 dynein. The MIA complex appears to regulate I1 dynein and possibly outer arm dyneins, which are both essential for normal motility.

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Fox, L. A., and W. S. Sale. "Direction of force generated by the inner row of dynein arms on flagellar microtubules." Journal of Cell Biology 105, no. 4 (October 1, 1987): 1781–87. http://dx.doi.org/10.1083/jcb.105.4.1781.

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Our goal was to determine the direction of force generation of the inner dynein arms in flagellar axonemes. We developed an efficient means of extracting the outer row of dynein arms in demembranated sperm tail axonemes, leaving the inner row of dynein arms structurally and functionally intact. Sperm tail axonemes depleted of outer arms beat at half the beat frequency of sperm tails with intact arms over a wide range of ATP concentrations. The isolated, outer arm-depleted axonemes were induced to undergo microtubule sliding in the presence of ATP and trypsin. Electron microscopic analysis of the relative direction of microtubule sliding (see Sale, W. S. and P. Satir, 1977, Proc. Natl. Acad. Sci. USA, 74:2045-2049) revealed that the doublet microtubule with the row of inner dynein arms, doublet N, always moved by sliding toward the proximal end of the axoneme relative to doublet N + 1. Therefore, the inner arms generate force such that doublet N pushes doublet N + 1 tipward. This is the same direction of microtubule sliding induced by ATP and trypsin in axonemes having both inner and outer dynein arms. The implications of this result for the mechanism of ciliary bending and utility in functional definition of cytoplasmic dyneins are discussed.

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Bui, Khanh Huy, Hitoshi Sakakibara, Tandis Movassagh, Kazuhiro Oiwa, and Takashi Ishikawa. "Asymmetry of inner dynein arms and inter-doublet links in Chlamydomonas flagella." Journal of Cell Biology 186, no. 3 (August 10, 2009): 437–46. http://dx.doi.org/10.1083/jcb.200903082.

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Although the widely shared “9 + 2” structure of axonemes is thought to be highly symmetrical, axonemes show asymmetrical bending during planar and conical motion. In this study, using electron cryotomography and single particle averaging, we demonstrate an asymmetrical molecular arrangement of proteins binding to the nine microtubule doublets in Chlamydomonas reinhardtii flagella. The eight inner arm dynein heavy chains regulate and determine flagellar waveform. Among these, one heavy chain (dynein c) is missing on one microtubule doublet (this doublet also lacks the outer dynein arm), and another dynein heavy chain (dynein b or g) is missing on the adjacent doublet. Some dynein heavy chains either show an abnormal conformation or were replaced by other proteins, possibly minor dyneins. In addition to nexin, there are two additional linkages between specific pairs of doublets. Interestingly, all these exceptional arrangements take place on doublets on opposite sides of the axoneme, suggesting that the transverse functional asymmetry of the axoneme causes an in-plane bending motion.

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Ishibashi, Kenta, Hitoshi Sakakibara, and Kazuhiro Oiwa. "Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble." International Journal of Molecular Sciences 21, no. 8 (April 18, 2020): 2843. http://dx.doi.org/10.3390/ijms21082843.

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In eukaryotic cilia and flagella, various types of axonemal dyneins orchestrate their distinct functions to generate oscillatory bending of axonemes. The force-generating mechanism of dyneins has recently been well elucidated, mainly in cytoplasmic dyneins, thanks to progress in single-molecule measurements, X-ray crystallography, and advanced electron microscopy. These techniques have shed light on several important questions concerning what conformational changes accompany ATP hydrolysis and whether multiple motor domains are coordinated in the movements of dynein. However, due to the lack of a proper expression system for axonemal dyneins, no atomic coordinates of the entire motor domain of axonemal dynein have been reported. Therefore, a substantial amount of knowledge on the molecular architecture of axonemal dynein has been derived from electron microscopic observations on dynein arms in axonemes or on isolated axonemal dynein molecules. This review describes our current knowledge and perspectives of the force-generating mechanism of axonemal dyneins in solo and in ensemble.

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Bui, Khanh Huy, Hitoshi Sakakibara, Tandis Movassagh, Kazuhiro Oiwa, and Takashi Ishikawa. "Molecular architecture of inner dynein arms in situ in Chlamydomonas reinhardtii flagella." Journal of Cell Biology 183, no. 5 (November 24, 2008): 923–32. http://dx.doi.org/10.1083/jcb.200808050.

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The inner dynein arm regulates axonemal bending motion in eukaryotes. We used cryo-electron tomography to reconstruct the three-dimensional structure of inner dynein arms from Chlamydomonas reinhardtii. All the eight different heavy chains were identified in one 96-nm periodic repeat, as expected from previous biochemical studies. Based on mutants, we identified the positions of the AAA rings and the N-terminal tails of all the eight heavy chains. The dynein f dimer is located close to the surface of the A-microtubule, whereas the other six heavy chain rings are roughly colinear at a larger distance to form three dyads. Each dyad consists of two heavy chains and has a corresponding radial spoke or a similar feature. In each of the six heavy chains (dynein a, b, c, d, e, and g), the N-terminal tail extends from the distal side of the ring. To interact with the B-microtubule through stalks, the inner-arm dyneins must have either different handedness or, more probably, the opposite orientation of the AAA rings compared with the outer-arm dyneins.

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King, Stephen M. "Axonemal Dynein Arms." Cold Spring Harbor Perspectives in Biology 8, no. 11 (August 15, 2016): a028100. http://dx.doi.org/10.1101/cshperspect.a028100.

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Smith, E. F., and W. S. Sale. "Structural and functional reconstitution of inner dynein arms in Chlamydomonas flagellar axonemes." Journal of Cell Biology 117, no. 3 (May 1, 1992): 573–81. http://dx.doi.org/10.1083/jcb.117.3.573.

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The inner row of dynein arms contains three dynein subforms. Each is distinct in composition and location in flagellar axonemes. To begin investigating the specificity of inner dynein arm assembly, we assessed the capability of isolated inner arm dynein subforms to rebind to their appropriate positions on axonemal doublet microtubules by recombining them with either mutant or extracted axonemes missing some or all dyneins. Densitometry of Coomassie blue-stained polyacrylamide gels revealed that for each inner dynein arm subform, binding to axonemes was saturable and stoichiometric. Using structural markers of position and polarity, electron microscopy confirmed that subforms bound to the correct inner arm position. Inner arms did not bind to outer arm or inappropriate inner arm positions despite the availability of sites. These and previous observations implicate specialized tubulin isoforms or nontubulin proteins in designation of specific inner dynein arm binding sites. Further, microtubule sliding velocities were restored to dynein-depleted axonemes upon rebinding of the missing inner arm subtypes as evaluated by an ATP-induced microtubule sliding disintegration assay. Therefore, not only were the inner arm dynein subforms able to identify and bind to the correct location on doublet microtubules but they bound in a functionally active conformation.

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Piperno, G., and Z. Ramanis. "The proximal portion of Chlamydomonas flagella contains a distinct set of inner dynein arms." Journal of Cell Biology 112, no. 4 (February 15, 1991): 701–9. http://dx.doi.org/10.1083/jcb.112.4.701.

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A specific type of inner dynein arm is located primarily or exclusively in the proximal portion of Chlamydomonas flagella. This dynein is absent from flagella less than 6 microns long, is assembled during the second half of flagellar regeneration time and is resistant to extraction under conditions causing complete solubilization of two inner arm heavy chains and partial solubilization of three other heavy chains. This and other evidence described in this report suggest that the inner arm row is composed of five distinct types of dynein arms. Therefore, the units of three inner arms that repeat every 96 nm along the axoneme are composed of different dyneins in the proximal and distal portions of flagella.

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Dissertations / Theses on the topic "Dynein arms"

1

Zhao, Jingmin. "Targetd Gene Knockout of the Outer Arm Dynein Heavy Chain Alpha Gene Causes Loss of Outer Arms and Decreased Beat Frequency in Tetrahymena Thermophila." Miami University / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=miami1174938168.

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Thomas, Lucie. "Bases moléculaires et cellulaires de l'assemblage de l'axonème des cils mobiles." Electronic Thesis or Diss., Sorbonne université, 2023. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2023SORUS097.pdf.

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Les bras de dynéine (BDs), moteurs du mouvement ciliaire et flagellaire, sont ancrés à intervalles réguliers le long de l'axonème des cils mobiles et des flagelles. Les dyskinésies ciliaires primitives (DCP) sont des maladies respiratoires rares, de transmission essentiellement autosomique récessive, liées à un défaut des cils mobiles, souvent associées à une infertilité masculine. Environ 25% des patients DCP présentent une absence des BDs externes et internes. Ces patients portent des mutations dans un des 13 gènes impliqués qui codent, pour la plupart, des constituants des complexes cytoplasmiques d'assemblage des BDs. L'objectif de cette thèse était de préciser le rôle de deux co-chaperonnes appartenant au(x) complexe(s) d'assemblage cytoplasmique des BDs, codées par des gènes nouvellement (TTC12) ou récemment (PIH1D3) impliqués dans les DCP. Nos travaux sur TTC12 ont révélé pour la première fois l'existence de mécanismes d'assemblage des BDs différents entre les cils mobiles et les flagelles chez l'Homme, expliquant le phénotype particulier de ces patients : infertilité masculine prédominante et atteinte respiratoire modérée. Nos données démontrent également l'existence de mécanismes d'assemblage distincts entre les différents sous-types de BDs internes. Ces travaux nous ont conduits à développer un modèle de cellules épithéliales nasales humaines (CENH) différenciées in vitro en interface air-liquide avec invalidation de gène par CRISPR-Cas9. Cet outil ouvre de nouvelles perspectives pour l'étude de la physiopathologie de maladies respiratoires. Notre étude sur PIH1D3, responsable de la seule DCP non syndromique récessive liée à l'X, a montré que les femmes porteuses hétérozygotes d'un défaut de PIH1D3 présentaient des symptômes respiratoires variables (absents à sévères) en relation avec le taux d'inactivation du chromosome X qui porte l'allèle muté. Ce taux d'inactivation a été déterminé par l'évaluation de la méthylation des dimères CG selon deux approches : digestion enzymatique au locus HUMARA et conversion au bisulfite au locus PIH1D3. Ces résultats incitent donc à rechercher une mutation hétérozygote de PIH1D3, en vue d'un conseil génétique, chez (i) des femmes apparentées aux patients masculins avec DCP liée à PIH1D3, et (ii) des femmes avec infections respiratoires chroniques sans étiologie identifiée. Dans les deux cas, le diagnostic de DCP est difficile à porter chez ces femmes : absence de l'infertilité masculine, du situs inversus, signes respiratoires modérés, NO nasal normal. Ce travail indique que dans la perspective d'une thérapie génique ou ARN, une compensation d'environ 30% du niveau de l'expression de PIH1D3 pourrait améliorer significativement le phénotype respiratoire des patients
Dynein arms (DAs), the motors of ciliary and flagella beating, are anchored with a regular spacing along cilia and flagella axonemes. Primary ciliary dyskinesia (PCD) is a rare respiratory disease due to defects in motile cilia. This mainly recessive condition combines laterality defects in half of the patients and frequent male and female hypofertility. About 25% of PCD patients show an absence of both outer and inner DAs. Those patients carry mutations in one of the 13 implicated genes that drive, for most of them, the cytoplasmic assembly of DAs. The aim of this thesis was to clarify the role of two co-chaperones, part of the cytoplasmic DA assembly complexes and encoded by PCD genes newly (TTC12) or recently (PIH1D3) identified. Our work on TTC12 revealed for the first time the existence of different mechanisms of DA assembly between respiratory cilia and sperm flagella in humans. This is in keeping with the peculiar phenotype of patients with TTC12 mutations: a predominant male infertility associated with mild respiratory signs. Our data also show the existence of a distinct DA assembly process for the different subspecies of inner DAs. Within the framework of this study, we developed an original cellular model of human airway epithelial cells (HAECs) differentiated in vitro at air-liquid interface, in which genes can be CRISPR-Cas9-invalidated. This tool opens new avenues for the study of the pathophysiology of airway diseases. Our study on PIH1D3, which mutations underlie the unique known X-linked non-syndromic PCD, showed that women who carry a heterozygous PIH1D3 mutation displayed variable airway phenotypes (from asymptomatic to severe respiratory symptoms) in close relation to the X-inactivation rate of the mutated allele. This has been shown by two approaches that assess DNA methylation of CG dimers: enzymatic digestion at the HUMARA locus and bisulfite conversion at the PIH1D3 locus. Those results prompt to search for heterozygous mutations in PIH1D3, in anticipation of a genetic counselling, in (i) females relatives of male PCD patients with a PIH1D3 defect, and (ii) females with mild chronic respiratory symptoms of unknown etiology. In both cases, diagnosis is difficult to estabilsh in those women given the absence of situs inversus, mild respiratory signs, and normal nasal NO. At the prospect of gene or RNA therapy, this work suggests that reaching 30% of PIH1D3 expression could significantly improve the airway phenotype in patients

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Liu, Siming. "TESTING THE MULTI-DYNEIN HYPOTHESIS BY MUTATING INNER ARM DYNEIN HEAVY CHAINS IN TETRAHYMENA THERMOPHILA." Miami University / OhioLINK, 2004. http://rave.ohiolink.edu/etdc/view?acc_num=miami1077152822.

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Kinzel, Kathryn Whitney. "Functional analysis of inner-arm dynein knockdowns in Trypanosoma brucei /." Connect to online version, 2008. http://ada.mtholyoke.edu/setr/websrc/pdfs/www/2008/268.pdf.

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Deckman, Cassandra M. "DEPHOSPHORYLATION OF INNER ARM 1 IS REQUIRED FOR CILIARY REVERSALS IN TETRAHYMENA THERMOPHILA." Miami University / OhioLINK, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=miami1054064051.

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Casey, Diane M. "DC3, a Calcium-Binding Protein Important for Assembly of the Chlamydomonas Outer Dynein Arm: a Dissertation." eScholarship@UMMS, 2005. http://escholarship.umassmed.edu/gsbs_diss/156.

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The outer dynein arm-docking complex (ODA-DC) specifies the outer dynein arm-binding site on the flagellar axoneme. The ODA-DC of Chlamydomonas contains equimolar amounts of three proteins termed DC1, DC2, and DC3 (Takada et al., 2002). DC1 and DC2 are predicted to be coiled-coil proteins, and are encoded by ODA3 and ODA1, respectively (Koutoulis et al., 1997; Takada et al., 2002). Prior to this work, nothing was known about DC3. To fully understand the function(s) of the ODA-DC, a detailed analysis of each of its component parts is necessary. To that end, this dissertation describes the characterization of the smallest subunit, DC3. In Chapter II, I report the isolation and sequencing of genomic and full-length cDNA clones encoding DC3. The sequence predicts a 21,341 D protein with four EF hands that is a member of the CTER (Calmodulin, Troponin C, Essential and Regulatory myosin light chains) group and is most closely related to a predicted protein from Plasmodium. The DC3 gene, termed ODA14, is intronless. Chlamydomonas mutants that lack DC3 exhibit slow, jerky swimming due to loss of some but not all, outer dynein arms. Some outer doublet microtubules without arms had a "partial" docking complex, indicating that DC1 and DC2 can assemble in the absence of DC3. In contrast, DC3 cannot assemble in the absence of DC1 or DC2. Transformation of a DC3-deletion strain with the wild-type DC3 gene rescued both the motility phenotype and the structural defect, whereas a mutated DC3 gene was incompetent to rescue. The results indicate that DC3 is important for both outer arm and ODA-DC assembly. As mentioned above, DC3 has four EF-hands: two fit the consensus pattern for calcium binding and one contains two cysteine residues within its binding loop. To determine if the consensus EF-hands are functional, I purified bacterially expressed wild-type DC3 and analyzed its calcium-binding potential in the presence and absence of DTT and Mg2+. As reported in Chapter III, the protein bound one calcium ion with an affinity (Kd) of ~1 x 10-5 M. Calcium binding was observed only in the presence of DTT and thus is redox sensitive. DC3 also bound Mg2+ at physiological concentrations, but with a much lower affinity. Changing the essential glutamate to glutamine in both EF-hands eliminated the calcium-binding activity of the bacterially expressed protein. To investigate the role of the EF hands in vivo, I transformed the modified DC3 gene into a Chlamydomonas insertional mutant lacking DC3. The transformed strain swam normally, assembled a normal number of outer arms, and had a normal photoshock response, indicating that the E to Q mutations did not affect ODA-DC assembly, outer arm assembly, or Ca2+-mediated outer arm activity. Thus, DC3 is a true calcium-binding protein, but the function of this activity remains obscure. In Chapter IV, I report the initial characterization of a DC3 insertional mutant having a phenotype intermediate between that of the DC3-deletion strain and wild type. Furthermore, I suggest future experiments that may help elucidate the specific role of DC3 in outer arm assembly and ODA-DC function. Lastly, I speculate that the ODA-DC may play a role in flagellar regeneration.

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Casey, Diane M. "DC3, a Calcium-Binding Protein Important for Assembly of the Chlamydomonas Outer Dynein Arm: a Dissertation." eScholarship@UMMS, 2003. https://escholarship.umassmed.edu/gsbs_diss/156.

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The outer dynein arm-docking complex (ODA-DC) specifies the outer dynein arm-binding site on the flagellar axoneme. The ODA-DC of Chlamydomonas contains equimolar amounts of three proteins termed DC1, DC2, and DC3 (Takada et al., 2002). DC1 and DC2 are predicted to be coiled-coil proteins, and are encoded by ODA3 and ODA1, respectively (Koutoulis et al., 1997; Takada et al., 2002). Prior to this work, nothing was known about DC3. To fully understand the function(s) of the ODA-DC, a detailed analysis of each of its component parts is necessary. To that end, this dissertation describes the characterization of the smallest subunit, DC3. In Chapter II, I report the isolation and sequencing of genomic and full-length cDNA clones encoding DC3. The sequence predicts a 21,341 D protein with four EF hands that is a member of the CTER (Calmodulin, Troponin C, Essential and Regulatory myosin light chains) group and is most closely related to a predicted protein from Plasmodium. The DC3 gene, termed ODA14, is intronless. Chlamydomonas mutants that lack DC3 exhibit slow, jerky swimming due to loss of some but not all, outer dynein arms. Some outer doublet microtubules without arms had a "partial" docking complex, indicating that DC1 and DC2 can assemble in the absence of DC3. In contrast, DC3 cannot assemble in the absence of DC1 or DC2. Transformation of a DC3-deletion strain with the wild-type DC3 gene rescued both the motility phenotype and the structural defect, whereas a mutated DC3 gene was incompetent to rescue. The results indicate that DC3 is important for both outer arm and ODA-DC assembly. As mentioned above, DC3 has four EF-hands: two fit the consensus pattern for calcium binding and one contains two cysteine residues within its binding loop. To determine if the consensus EF-hands are functional, I purified bacterially expressed wild-type DC3 and analyzed its calcium-binding potential in the presence and absence of DTT and Mg2+. As reported in Chapter III, the protein bound one calcium ion with an affinity (Kd) of ~1 x 10-5 M. Calcium binding was observed only in the presence of DTT and thus is redox sensitive. DC3 also bound Mg2+ at physiological concentrations, but with a much lower affinity. Changing the essential glutamate to glutamine in both EF-hands eliminated the calcium-binding activity of the bacterially expressed protein. To investigate the role of the EF hands in vivo, I transformed the modified DC3 gene into a Chlamydomonas insertional mutant lacking DC3. The transformed strain swam normally, assembled a normal number of outer arms, and had a normal photoshock response, indicating that the E to Q mutations did not affect ODA-DC assembly, outer arm assembly, or Ca2+-mediated outer arm activity. Thus, DC3 is a true calcium-binding protein, but the function of this activity remains obscure. In Chapter IV, I report the initial characterization of a DC3 insertional mutant having a phenotype intermediate between that of the DC3-deletion strain and wild type. Furthermore, I suggest future experiments that may help elucidate the specific role of DC3 in outer arm assembly and ODA-DC function. Lastly, I speculate that the ODA-DC may play a role in flagellar regeneration.

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KABI, AMRITA. "Role of Inner Arm Dyneins and Hydin in Ciliary Motility in Tetrahymena thermophila." Miami University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=miami1271977227.

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Lammers, Franziska Barbara [Verfasser], and Heymut [Akademischer Betreuer] Omran. "Identifizierung von isolierten Defekten des Inneren Dynein-Arm-Komplex bei Patienten mit Primärer Ciliärer Dyskinesie / Franziska Barbara Lammers ; Betreuer: Heymut Omran." Münster : Universitäts- und Landesbibliothek Münster, 2021. http://d-nb.info/1229992588/34.

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Wirschell, Maureen. "Chlamydomonas Reinhardtii ODA5 Encodes an Axonemal Protein Required for Assembly of the Outer Dynein Arm and an Associated Flagellar Adenylate Kinase: A Dissertation." eScholarship@UMMS, 2004. https://escholarship.umassmed.edu/gsbs_diss/25.

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The first type of dynein identified, axonemel dynein (Gibbons and Rowe, 1965), slides adjacent microtubules within the axoneme, generating the force necessary for ciliary and flagellar beating. The outer dynein arm is an important component of the flagellar axoneme, providing up to 60% of the force for flagellar motility. In the absence of the outer arm, cells swim with a slow-jerky motion at about 1/3rd the speed of wild-type cells, and the flagellar beat frequency is markedly reduced. Sixteen genes (ODA1-ODA16) have been identified that are required for outer arm assembly in Chlamydomonas reinhardtii. In addition, PF13, PF22, and FLA14 are required for outer dynein arm assembly, but their phenotypes are pleiotropic, suggesting that they affect additional flagellar components. Of the uncloned genes, ODA5, ODA8, and ODA10 are of particular interest because they do not encode subunits of the outer arm or the outer dynein arm-docking complex (ODA-DC). Mutant alleles of these genes are unable to complement in temporary dikaryons, suggesting that the gene products interact with each other (Kamiya, 1988). Since the genes encoding all of the known components of the outer dynein arm and the ODA-DC have been characterized, it is of great interest to identify the gene products of these additional, uncloned ODA alleles. The first chapter provides an introduction to the Chlamydomonasflagellum, the dyneins in general, the outer dynein arm in particular, and mutations that impinge on the assembly and regulation of this important axonemal structure. The second chapter addresses the identification and isolation of genomic DNA containing the ODA5 gene. Utilizing a NIT1-tagged oda5-insertional mutant, I identified sequences flanking the site of the inserted NIT1 gene. These sequences were used to isolate wild-type genomic clones spanning the ODA5 gene. When transformed into the oda5 mutant, the wild-type clones rescued the mutant phenotype. These results demonstrated the successful isolation of the ODA5 gene. The third chapter describes the identification of the ODA5 gene and its corresponding cDNA. The rescuing genomic fragments were sequenced. Gene modeling was used to predict intron-exon splice sites. Primers to predicted exons were designed and used to obtain the ODA5 cDNA. The gene structure of Oda5 was analyzed and its predicted amino acid sequence deduced. Secondary structure predictions indicate that Oda5p is likely to contain a series of coiled-coil domains, followed by a poly-glycine sequence and a short, highly charged region. Northern analysis demonstrated that ODA5 gene expression is upregulated by deflagellation, a hallmark of many flagellar mRNAs. Data in CHAPTER IV further characterize the Oda5 protein and its association with the axoneme. Oda5p localizes to the flagellum, consistent with the enhancement in mRNA levels in response to deflagellation. Within the flagellum, Oda5p is an axonemal component that is released from the axoneme upon high salt extraction, as are the ODA-DC and the outer dynein arm. However, Oda5p does not associate with this super-complex in the high salt extract as determined by sucrose gradient sedimentation. Oda5p assembles onto the axoneme independently of the outer dynein arm and the ODA-DC,demonstrating it does not require these complexes for localization. Furthermore, Oda5p assembles onto the axoneme in the oda8, but not the oda10 mutant, demonstrating a role for the Oda10 protein in localization of Oda5p. These data provide the first biochemical evidence for an interaction between Oda5p and Oda10p. CHAPTER V reveals the discovery of a previously unrecognized phenotype exhibited in both oda5 and oda10 mutant strains: a defect in the assembly of a previously unknown flagellar adenylate kinase (AK). The protein levels of this flagellar AK are reduced in oda5 mutant axonemes, as determined by quantitative mass spectrometry. Direct enzymatic assays confirmed a reduction in AK activity in both oda5 and oda10 mutant axonemes, providing a second line of biochemical evidence supporting a complex containing Oda5p and OdalOp. The sequence of the flagellar AK gene and its cDNA were determined. CHAPTER VI details our efforts to identify the ODA10 gene. Genomic clones were isolated, which contain sequences at, or near, the ODA10 locus. Analysis of the genomic clones yielded no insights into the identity of the ODA10 gene. The inability of these clones to rescue the Oda10-motility phenotype indicates that these clones most likely do not contain an intact ODA10 gene. And lastly, CHAPTER VII discusses future experimentation that can be done based on the data provided by the current study.

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Books on the topic "Dynein arms"

1

Kong, Xuejun. Biochemical analyses of axonemal dyneins from a wild-type Tetrahymena and a mutant Tetrahymena lacking outer dynein arms. 1993.

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Ludmann, Susan A. Biochemical and functional analyses of a mutant Tetrahymena thermophila that lacks outer dynein arms. 1993.

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Daigre, Jeanell Loretta. Biochemical and functional analyses of 22S dynein isolated from mutant Tetrahymena axonemes deficient in outer dynein arms. 1994.

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Dynix: A Guide for Librarians and Systems Managers. Taylor & Francis Group, 2018.

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Book chapters on the topic "Dynein arms"

1

Gibbons, Ian R. "Dynein, axonemal." In Guidebook to the Cytoskeletal and Motor Proteins, 381–85. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.00117.

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Abstract Axonemal dynein forms a double row of projections, the outer and inner arms, that are attached to the A tubule of each axonemal doublet and extend toward the B tubule of the adjacent doublet.10 The outer dynein arms are distributed along the length of the A tubule, with a constant spacing of 24 nm. The arrangement of inner dynein arms is more complex, with three distinct species of inner arm that are distributed along each A tubule in unevenly spaced triplets.

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Hwang, Juyeon, Emily L. Hunter, Winfield S. Sale, and Maureen Wirschell. "Control of axonemal inner dynein arms." In Dyneins, 270–97. Elsevier, 2018. http://dx.doi.org/10.1016/b978-0-12-809471-6.00009-7.

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Alford, Lea M., Maureen Wirschell, Ryosuke Yamamoto, and Winfield S. Sale. "Control of Axonemal Inner Dynein Arms." In Dyneins, 312–35. Elsevier, 2012. http://dx.doi.org/10.1016/b978-0-12-382004-4.10011-1.

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Smith, Elizabeth F. "Chapter 69 Reconstitution of Dynein Arms in Vitro." In Methods in Cell Biology, 491–96. Elsevier, 1995. http://dx.doi.org/10.1016/s0091-679x(08)60850-x.

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Conference papers on the topic "Dynein arms"

1

Bayly, P. V., B. L. Lewis, E. C. Ranz, R. J. Okamoto, R. B. Pless, and S. K. Dutcher. "Kinematics and Kinetics of Flagellar Locomotion in Chlamydomonas Reinhardtii." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53290.

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The forces exerted on the flagellum of the swimming alga Chlamydomonas reinhardtii by surrounding fluid are estimated from video data. “Wild-type” cells, as well as cells lacking inner dynein arms (ida3) and cells lacking outer dynein arms (oda2) were imaged (350 fps; 125 nm). Digital image registration and sorting algorithms provide high-resolution descriptions of the kinematics of the cell body and flagellum. The swimming cell is then modeled as an ellipsoid in Stokes flow, propelled by viscous forces that depend linearly on the velocity of the flagellum. The coefficients (CN and CT) that related normal and tangent forces on the flagellum to corresponding velocity components are estimated from equilibrium requirements. Their values are consistent among all three genotypes and similar to theoretical predictions.

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Zariwala, M., M. Leigh, M. Hazucha, S. Minnix, M. Armstrong, A. Lori, N. Loges, et al. "DNAH11Mutations Are a Common Cause of Primary Ciliary Dyskinesia (PCD) in Patients with Normal Ciliary Dynein Arms." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1213.

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Ueno, Hironori, Takuji Ishikawa, Khanh Huy Bui, Kohsuke Gonda, Takashi Ishikawa, and Takami Yamaguchi. "Analysis of Ciliary Motion and the Axonemal Structure in the Mouse Respiratory Cilia." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80232.

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Mucociliary clearance on the surface of the tracheal lumen is an important component of lung defense against dust mites and viruses. However, the axonemal structure that achieves effective ciliary motion and the mechanisms by which discretely distributed ciliary cells generate directional flow are unknown. In this study, we examined individual ciliary motion with 7–9-nm spatial precision by labeling the ciliary tip with quantum dots, and detected an asymmetric beating pattern. Cryo-electron tomography revealed that the densities of two inner dynein arms were missing from at least two doublet microtubules in the axonemal structure. Although the flow directions generated by individual ciliated cells were unsteady and diverse, the time- and space-averaged velocity field was found to be directional. These results indicate that the asymmetric ciliary motion is driven by the asymmetric axonemal structure, and it generates overall directional flow from the lungs to the oropharynx on sparsely distributed ciliated cells.

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Smith, A. J., X. M. Bustamante-Marin, L. E. Herring, W. N. Yin, P. R. Sears, M. W. Leigh, M. R. Knowles, M. A. Zariwala, and L. E. Ostrowski. "Investigating the Role of SPAG1 in the Cytoplasmic Assembly of Axonemal Dynein Arms: Genotypic and Phenotypic Variability of SPAG1 Mutations in Primary Ciliary Dyskinesia." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a1197.

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